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Merck
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Documenti fondamentali

SML1959

Sigma-Aldrich

GA3-AM

≥95% (HPLC)

Sinonimo/i:

(1α,2β,4aα,4bβ,10β)-2,4a,7-Trihydroxy-1-methyl-8-methylenegibb-3-ene-1,10-dicarboxylic Acid 1,4a-Lactone Acetoxymethyl Ester, (1S,2S,4aR,4bR,7S,9aS,10S,10aR)-1,2,4b,5,6,7,8,9,10,10a-decahydro-2,7-dihydroxy-1-methyl-8-methylene-13-oxo-4a,1-(Epoxymethano)-7,9a-methanobenz[a]azulene-10-acetic acid (acetyloxy)methyl ester, Gibberellic Acid Acetoxymethyl Ester

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About This Item

Formula empirica (notazione di Hill):
C22H26O8
Numero CAS:
Peso molecolare:
418.44
Codice UNSPSC:
12352200
NACRES:
NA.77

Livello qualitativo

Saggio

≥95% (HPLC)

Stato

powder

Colore

white to beige

Solubilità

DMSO: 2 mg/mL, clear

Temperatura di conservazione

−20°C

Azioni biochim/fisiol

GA3-AM is a cell permeable analog of the plant hormone gibberellic acid that acts as a chemical dimerizer or chemical inducer of dimerization. GA3 and rapamycin chemically inducible dimerization systems are orthogonal. GA3-AM has been used in conjunction with a rapamycin dimerization system and CRISPR/Cas9 activators for temporal control of CRISPR/Cas9 activator function, enabling temporal regulation of multiple genes.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Zehua Bao et al.
ACS synthetic biology, 6(4), 686-693 (2017-01-06)
The concerted action of multiple genes in a time-dependent manner controls complex cellular phenotypes, yet the temporal regulation of gene expressions is restricted on a single-gene level, which limits our ability to control higher-order gene networks and understand the consequences
Takafumi Miyamoto et al.
Nature chemical biology, 8(5), 465-470 (2012-03-27)
Using a newly synthesized gibberellin analog containing an acetoxymethyl group (GA(3)-AM) and its binding proteins, we developed an efficient chemically inducible dimerization (CID) system that is completely orthogonal to existing rapamycin-mediated protein dimerization. Combining the two systems should allow applications
Shameika R Wilmington et al.
PloS one, 11(4), e0152679-e0152679 (2016-04-05)
A common way to study protein function is to deplete the protein of interest from cells and observe the response. Traditional methods involve disrupting gene expression but these techniques are only effective against newly synthesized proteins and leave previously existing

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